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LongText Report for: 4Q82-pdb

Name Class
4Q82-pdb
HEADER    HYDROLASE                               25-APR-14   4Q82              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOLIPASE/CARBOXYLESTERASE FROM HALIANGIUM   
TITLE    2 OCHRACEUM                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOLIPASE/CARBOXYLESTERASE;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALIANGIUM OCHRACEUM;                           
SOURCE   3 ORGANISM_TAXID: 502025;                                              
SOURCE   4 STRAIN: DSM 14365;                                                   
SOURCE   5 GENE: HOCH_6203;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21DE3 GOLD;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG68                                   
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL       
KEYWDS   2 GENOMICS, MCSG, ALPHA-BETA-FOLD, HYDROLASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,C.HATZOS-SKINTGES,M.ENDRES,A.JOACHIMIAK,MIDWEST CENTER FOR      
AUTHOR   2 STRUCTURAL GENOMICS (MCSG)                                           
REVDAT   1   14-MAY-14 4Q82    0                                                
JRNL        AUTH   Y.KIM,C.HATZOS-SKINTGES,M.ENDRES,A.JOACHIMIAK                
JRNL        TITL   CRYSTAL STRUCTURE OF PHOSPHOLIPASE/CARBOXYLESTERASE FROM     
JRNL        TITL 2 HALIANGIUM OCHRACEUM                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1678)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 66642                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3371                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.3068 -  5.3279    0.98     2878   121  0.1750 0.1857        
REMARK   3     2  5.3279 -  4.2303    1.00     2787   140  0.1234 0.1489        
REMARK   3     3  4.2303 -  3.6959    1.00     2722   155  0.1203 0.1365        
REMARK   3     4  3.6959 -  3.3582    1.00     2708   157  0.1355 0.1352        
REMARK   3     5  3.3582 -  3.1176    1.00     2676   156  0.1549 0.1674        
REMARK   3     6  3.1176 -  2.9338    1.00     2706   148  0.1684 0.2089        
REMARK   3     7  2.9338 -  2.7869    1.00     2697   139  0.1714 0.1956        
REMARK   3     8  2.7869 -  2.6656    1.00     2710   117  0.1725 0.2036        
REMARK   3     9  2.6656 -  2.5630    1.00     2665   154  0.1666 0.1958        
REMARK   3    10  2.5630 -  2.4746    1.00     2653   153  0.1667 0.1919        
REMARK   3    11  2.4746 -  2.3972    1.00     2691   146  0.1593 0.1710        
REMARK   3    12  2.3972 -  2.3287    1.00     2658   150  0.1546 0.1854        
REMARK   3    13  2.3287 -  2.2674    1.00     2651   154  0.1530 0.1836        
REMARK   3    14  2.2674 -  2.2121    1.00     2641   141  0.1521 0.1829        
REMARK   3    15  2.2121 -  2.1618    1.00     2679   143  0.1499 0.1782        
REMARK   3    16  2.1618 -  2.1158    1.00     2666   134  0.1455 0.1788        
REMARK   3    17  2.1158 -  2.0735    1.00     2656   146  0.1505 0.1801        
REMARK   3    18  2.0735 -  2.0343    1.00     2661   125  0.1564 0.1892        
REMARK   3    19  2.0343 -  1.9980    0.99     2625   143  0.1541 0.1997        
REMARK   3    20  1.9980 -  1.9641    0.99     2636   143  0.1523 0.1661        
REMARK   3    21  1.9641 -  1.9325    0.95     2543   128  0.1660 0.2011        
REMARK   3    22  1.9325 -  1.9027    0.93     2411   145  0.1730 0.1938        
REMARK   3    23  1.9027 -  1.8748    0.88     2376   113  0.1888 0.1890        
REMARK   3    24  1.8748 -  1.8483    0.82     2175   120  0.1916 0.2178        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.65                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           3850                                  
REMARK   3   ANGLE     :  1.270           5284                                  
REMARK   3   CHIRALITY :  0.063            542                                  
REMARK   3   PLANARITY :  0.007            728                                  
REMARK   3   DIHEDRAL  : 13.666           1368                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 57 through 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  55.4391  11.2688  41.0074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2695 T22:   0.2534                                     
REMARK   3      T33:   0.3693 T12:   0.0888                                     
REMARK   3      T13:   0.2906 T23:   0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4587 L22:   2.8873                                     
REMARK   3      L33:   2.2613 L12:  -0.9838                                     
REMARK   3      L13:  -0.4107 L23:   0.6047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1345 S12:  -0.2343 S13:  -0.2734                       
REMARK   3      S21:   0.5298 S22:   0.0553 S23:   0.8296                       
REMARK   3      S31:   0.1841 S32:  -0.5847 S33:   0.3471                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 86 through 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  56.5205  12.4842  32.5068              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1555 T22:   0.2065                                     
REMARK   3      T33:   0.3520 T12:   0.0444                                     
REMARK   3      T13:   0.0801 T23:   0.0341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4413 L22:   0.8515                                     
REMARK   3      L33:   3.1361 L12:   0.6636                                     
REMARK   3      L13:  -0.5006 L23:   1.0245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.0953 S13:  -0.0549                       
REMARK   3      S21:   0.1615 S22:  -0.0406 S23:   0.7277                       
REMARK   3      S31:  -0.1169 S32:  -0.5732 S33:   0.1291                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 107 through 120 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  67.6101   3.8858  42.5019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4609 T22:   0.2260                                     
REMARK   3      T33:   0.1990 T12:   0.0854                                     
REMARK   3      T13:   0.1071 T23:   0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9947 L22:   1.9453                                     
REMARK   3      L33:   0.9173 L12:   0.8546                                     
REMARK   3      L13:  -0.1076 L23:  -1.1351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0818 S12:  -0.4066 S13:  -0.0810                       
REMARK   3      S21:   0.9596 S22:  -0.0344 S23:   0.3087                       
REMARK   3      S31:   0.2076 S32:   0.0669 S33:   0.0871                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 121 through 138 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.0695  19.2332  35.4559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1894 T22:   0.1578                                     
REMARK   3      T33:   0.1516 T12:   0.0513                                     
REMARK   3      T13:   0.0941 T23:   0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5308 L22:   3.7602                                     
REMARK   3      L33:   3.6679 L12:  -0.0454                                     
REMARK   3      L13:  -0.4980 L23:   2.5013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:  -0.3205 S13:   0.3174                       
REMARK   3      S21:   0.3542 S22:   0.0604 S23:   0.1069                       
REMARK   3      S31:  -0.2998 S32:   0.0244 S33:  -0.0403                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 139 through 173 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  56.4623   2.9146  30.1537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1817 T22:   0.2195                                     
REMARK   3      T33:   0.4448 T12:  -0.0364                                     
REMARK   3      T13:   0.0740 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6793 L22:   0.9709                                     
REMARK   3      L33:   2.4820 L12:  -0.0417                                     
REMARK   3      L13:  -0.7736 L23:   0.3547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1724 S12:   0.0090 S13:  -0.4253                       
REMARK   3      S21:   0.2937 S22:   0.0067 S23:   0.7822                       
REMARK   3      S31:   0.3766 S32:  -0.4202 S33:   0.0803                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 174 through 209 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.6959   4.0620  21.0049              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1427 T22:   0.1234                                     
REMARK   3      T33:   0.2097 T12:   0.0144                                     
REMARK   3      T13:  -0.0364 T23:  -0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8176 L22:   2.7496                                     
REMARK   3      L33:   2.9297 L12:  -0.1355                                     
REMARK   3      L13:  -0.9892 L23:   0.1283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0675 S12:   0.1791 S13:  -0.3438                       
REMARK   3      S21:  -0.2141 S22:  -0.0323 S23:   0.5199                       
REMARK   3      S31:   0.2809 S32:  -0.2728 S33:   0.0575                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 210 through 263 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  69.4870   8.8981  12.8431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2533 T22:   0.1866                                     
REMARK   3      T33:   0.1272 T12:   0.0636                                     
REMARK   3      T13:  -0.0703 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5068 L22:   1.9467                                     
REMARK   3      L33:   1.4827 L12:  -0.0081                                     
REMARK   3      L13:  -0.0787 L23:  -0.2436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1639 S12:   0.3380 S13:  -0.1065                       
REMARK   3      S21:  -0.6441 S22:  -0.1389 S23:   0.1591                       
REMARK   3      S31:   0.0432 S32:  -0.2011 S33:  -0.0270                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 264 through 292 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  68.3469  17.3627  23.8211              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1272 T22:   0.0956                                     
REMARK   3      T33:   0.0962 T12:   0.0446                                     
REMARK   3      T13:  -0.0046 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7118 L22:   2.7592                                     
REMARK   3      L33:   1.9902 L12:   0.4292                                     
REMARK   3      L13:  -0.2076 L23:   0.0292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0980 S12:  -0.0131 S13:  -0.0267                       
REMARK   3      S21:  -0.0563 S22:  -0.0747 S23:   0.2380                       
REMARK   3      S31:  -0.0782 S32:  -0.1680 S33:  -0.0228                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid 60 through 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  96.1756  37.0181   6.2286              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1378 T22:   0.4461                                     
REMARK   3      T33:   0.2590 T12:  -0.0901                                     
REMARK   3      T13:   0.0209 T23:   0.0568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6845 L22:   4.3211                                     
REMARK   3      L33:   2.2037 L12:   0.8869                                     
REMARK   3      L13:   0.2784 L23:  -1.2056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0877 S12:   0.5664 S13:   0.1143                       
REMARK   3      S21:  -0.4319 S22:  -0.0428 S23:  -0.9461                       
REMARK   3      S31:  -0.1417 S32:   0.7687 S33:   0.1471                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid 86 through 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  87.4443  34.2198   5.1772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1122 T22:   0.2876                                     
REMARK   3      T33:   0.1433 T12:  -0.0326                                     
REMARK   3      T13:  -0.0026 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4153 L22:   1.3049                                     
REMARK   3      L33:   4.4787 L12:  -0.4021                                     
REMARK   3      L13:  -0.1115 L23:  -1.5320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0143 S12:   0.5441 S13:  -0.0097                       
REMARK   3      S21:  -0.1538 S22:   0.0529 S23:  -0.3695                       
REMARK   3      S31:   0.2190 S32:   0.3988 S33:  -0.0267                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resid 107 through 120 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  96.9323  41.5200  17.6239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1903 T22:   0.3410                                     
REMARK   3      T33:   0.3325 T12:  -0.0908                                     
REMARK   3      T13:  -0.1280 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9466 L22:   4.3773                                     
REMARK   3      L33:   2.5292 L12:   1.2042                                     
REMARK   3      L13:   0.9520 L23:   0.4443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0644 S12:   0.0425 S13:   0.0158                       
REMARK   3      S21:   0.2400 S22:  -0.1536 S23:  -0.7419                       
REMARK   3      S31:  -0.1330 S32:   0.6244 S33:  -0.1861                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resid 121 through 138 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  89.7332  27.0747  12.2570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0896 T22:   0.2076                                     
REMARK   3      T33:   0.2079 T12:   0.0039                                     
REMARK   3      T13:  -0.0056 T23:   0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1239 L22:   5.1592                                     
REMARK   3      L33:   5.3894 L12:  -1.3412                                     
REMARK   3      L13:  -0.1844 L23:   0.0533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1080 S12:   0.0287 S13:  -0.5993                       
REMARK   3      S21:   0.2394 S22:   0.0215 S23:  -0.4968                       
REMARK   3      S31:   0.5326 S32:   0.5667 S33:  -0.0225                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'B' and (resid 139 through 209 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  81.0059  43.0650   8.1547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1946 T22:   0.2145                                     
REMARK   3      T33:   0.1714 T12:  -0.0558                                     
REMARK   3      T13:  -0.0602 T23:   0.0956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7655 L22:   1.3133                                     
REMARK   3      L33:   1.9431 L12:   0.3163                                     
REMARK   3      L13:  -0.0831 L23:  -0.2037                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1890 S12:   0.4429 S13:   0.5723                       
REMARK   3      S21:  -0.0558 S22:   0.0627 S23:  -0.0729                       
REMARK   3      S31:  -0.4394 S32:   0.1773 S33:   0.0528                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'B' and (resid 210 through 263 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  66.9382  38.4007  16.4082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1453 T22:   0.1364                                     
REMARK   3      T33:   0.1435 T12:   0.0478                                     
REMARK   3      T13:  -0.0210 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1317 L22:   2.2718                                     
REMARK   3      L33:   1.7782 L12:   0.1467                                     
REMARK   3      L13:  -0.2322 L23:  -0.1617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1036 S12:   0.1122 S13:   0.3119                       
REMARK   3      S21:   0.1565 S22:   0.0164 S23:   0.3066                       
REMARK   3      S31:  -0.3309 S32:  -0.2097 S33:   0.0779                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'B' and (resid 264 through 292 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  77.5193  29.1507  16.0397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0953 T22:   0.1102                                     
REMARK   3      T33:   0.0826 T12:   0.0136                                     
REMARK   3      T13:  -0.0054 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1696 L22:   2.2958                                     
REMARK   3      L33:   2.2171 L12:   0.2798                                     
REMARK   3      L13:  -0.1559 L23:  -0.0748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:   0.0988 S13:  -0.0510                       
REMARK   3      S21:   0.1427 S22:  -0.0305 S23:  -0.0579                       
REMARK   3      S31:  -0.0278 S32:   0.0918 S33:   0.1271                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Q82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085721.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67799                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200   FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.64000                            
REMARK 200   FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,DM                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS TRIS PROPANE PH7.0, 1.8 M      
REMARK 280  MAGNESIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 100K  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       38.96750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       73.04200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.96750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       73.04200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THERE ARE TWO MONOMERS IN THE ASYMMETRIC UNIT.               
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 640  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 572  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ASP A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     VAL A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ILE A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     VAL A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     ASP A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     ASN A    53                                                      
REMARK 465     GLN A    54                                                      
REMARK 465     ILE A    55                                                      
REMARK 465     ASP A    56                                                      
REMARK 465     SER B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ASP B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     ASP B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     THR B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     ALA B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     VAL B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     ILE B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     VAL B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     ASP B    44                                                      
REMARK 465     PRO B    45                                                      
REMARK 465     ILE B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     ASN B    53                                                      
REMARK 465     GLN B    54                                                      
REMARK 465     ILE B    55                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     ALA B    57                                                      
REMARK 465     MSE B    58                                                      
REMARK 465     VAL B    59                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     2ZC A 180    C1   C2   C3   C4   C5   C6   C7                    
REMARK 470     2ZC A 180    C8   N1                                             
REMARK 470     2ZC B 180    OD2  OD1  C1   C2   C3   C4   C5                    
REMARK 470     2ZC B 180    C6   C7   C8   N1                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    2ZC A 180     -123.16     56.85                                   
REMARK 500    2ZC B 180     -127.49     53.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A  138     VAL A  139                  149.24                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MCSG-APC103461   RELATED DB: TARGETTRACK                 
DBREF  4Q82 A   19   292  UNP    D0LMJ0   D0LMJ0_HALO1    19    292             
DBREF  4Q82 B   19   292  UNP    D0LMJ0   D0LMJ0_HALO1    19    292             
SEQADV 4Q82 SER A   16  UNP  D0LMJ0              EXPRESSION TAG                 
SEQADV 4Q82 ASN A   17  UNP  D0LMJ0              EXPRESSION TAG                 
SEQADV 4Q82 ALA A   18  UNP  D0LMJ0              EXPRESSION TAG                 
SEQADV 4Q82 SER B   16  UNP  D0LMJ0              EXPRESSION TAG                 
SEQADV 4Q82 ASN B   17  UNP  D0LMJ0              EXPRESSION TAG                 
SEQADV 4Q82 ALA B   18  UNP  D0LMJ0              EXPRESSION TAG                 
SEQRES   1 A  277  SER ASN ALA ASP ASP GLY GLY ASP ASP GLY GLY ALA GLU          
SEQRES   2 A  277  THR ASP ALA ALA VAL ALA ILE ASP ALA SER PRO VAL ASP          
SEQRES   3 A  277  ALA PRO ASP PRO ILE ASP ALA ALA PRO ASP ALA ASN GLN          
SEQRES   4 A  277  ILE ASP ALA MSE VAL ASP ASP ARG PRO SER SER ALA ARG          
SEQRES   5 A  277  LEU SER VAL ARG ALA LEU ASP THR THR GLU ALA GLY ASN          
SEQRES   6 A  277  GLY PHE TRP GLU TYR LEU PRO PRO ARG TYR GLY ALA GLU          
SEQRES   7 A  277  PRO ALA PRO LEU MSE VAL PHE TRP HIS GLY ILE GLY GLU          
SEQRES   8 A  277  ASN GLY ASP GLY SER GLU ALA ALA LEU ASP LYS VAL LEU          
SEQRES   9 A  277  ALA ASN GLY PRO PRO ARG TYR ILE GLU ARG ASP GLU TRP          
SEQRES  10 A  277  SER ASN GLU ARG PRO PHE VAL VAL LEU SER PRO GLN HIS          
SEQRES  11 A  277  ALA GLY GLY GLY CYS PRO SER ALA ASP GLU ILE ARG ASP          
SEQRES  12 A  277  PHE LEU ALA PHE ALA VAL ASP THR TYR GLU VAL ASP GLU          
SEQRES  13 A  277  SER ARG ILE TYR LEU THR GLY LEU 2ZC CYS GLY ALA ILE          
SEQRES  14 A  277  GLY SER TRP ASN TYR LEU ARG ALA HIS LEU ASP THR THR          
SEQRES  15 A  277  PRO ILE ALA ALA ALA VAL LEU ILE ALA GLY ASN GLY ARG          
SEQRES  16 A  277  PRO ALA PHE ASN ASP HIS GLY CYS ASP LEU ALA GLN VAL          
SEQRES  17 A  277  PRO ILE TRP GLY PHE HIS GLY ASP ALA ASP PRO THR VAL          
SEQRES  18 A  277  ALA PRO ALA GLY THR ILE GLU PRO MSE ASN GLY LEU ILE          
SEQRES  19 A  277  ALA CYS ALA GLN PRO ARG ALA ASP GLN GLN LEU THR VAL          
SEQRES  20 A  277  TYR GLU GLY VAL GLY HIS ASP SER TRP SER ARG THR TYR          
SEQRES  21 A  277  SER LEU SER ALA GLY HIS ASP ILE TYR ALA TRP LEU LEU          
SEQRES  22 A  277  SER GLN SER ARG                                              
SEQRES   1 B  277  SER ASN ALA ASP ASP GLY GLY ASP ASP GLY GLY ALA GLU          
SEQRES   2 B  277  THR ASP ALA ALA VAL ALA ILE ASP ALA SER PRO VAL ASP          
SEQRES   3 B  277  ALA PRO ASP PRO ILE ASP ALA ALA PRO ASP ALA ASN GLN          
SEQRES   4 B  277  ILE ASP ALA MSE VAL ASP ASP ARG PRO SER SER ALA ARG          
SEQRES   5 B  277  LEU SER VAL ARG ALA LEU ASP THR THR GLU ALA GLY ASN          
SEQRES   6 B  277  GLY PHE TRP GLU TYR LEU PRO PRO ARG TYR GLY ALA GLU          
SEQRES   7 B  277  PRO ALA PRO LEU MSE VAL PHE TRP HIS GLY ILE GLY GLU          
SEQRES   8 B  277  ASN GLY ASP GLY SER GLU ALA ALA LEU ASP LYS VAL LEU          
SEQRES   9 B  277  ALA ASN GLY PRO PRO ARG TYR ILE GLU ARG ASP GLU TRP          
SEQRES  10 B  277  SER ASN GLU ARG PRO PHE VAL VAL LEU SER PRO GLN HIS          
SEQRES  11 B  277  ALA GLY GLY GLY CYS PRO SER ALA ASP GLU ILE ARG ASP          
SEQRES  12 B  277  PHE LEU ALA PHE ALA VAL ASP THR TYR GLU VAL ASP GLU          
SEQRES  13 B  277  SER ARG ILE TYR LEU THR GLY LEU 2ZC CYS GLY ALA ILE          
SEQRES  14 B  277  GLY SER TRP ASN TYR LEU ARG ALA HIS LEU ASP THR THR          
SEQRES  15 B  277  PRO ILE ALA ALA ALA VAL LEU ILE ALA GLY ASN GLY ARG          
SEQRES  16 B  277  PRO ALA PHE ASN ASP HIS GLY CYS ASP LEU ALA GLN VAL          
SEQRES  17 B  277  PRO ILE TRP GLY PHE HIS GLY ASP ALA ASP PRO THR VAL          
SEQRES  18 B  277  ALA PRO ALA GLY THR ILE GLU PRO MSE ASN GLY LEU ILE          
SEQRES  19 B  277  ALA CYS ALA GLN PRO ARG ALA ASP GLN GLN LEU THR VAL          
SEQRES  20 B  277  TYR GLU GLY VAL GLY HIS ASP SER TRP SER ARG THR TYR          
SEQRES  21 B  277  SER LEU SER ALA GLY HIS ASP ILE TYR ALA TRP LEU LEU          
SEQRES  22 B  277  SER GLN SER ARG                                              
MODRES 4Q82 MSE A   58  MET  SELENOMETHIONINE                                   
MODRES 4Q82 MSE A   98  MET  SELENOMETHIONINE                                   
MODRES 4Q82 2ZC A  180  SER                                                     
MODRES 4Q82 MSE A  245  MET  SELENOMETHIONINE                                   
MODRES 4Q82 MSE B   98  MET  SELENOMETHIONINE                                   
MODRES 4Q82 2ZC B  180  SER                                                     
MODRES 4Q82 MSE B  245  MET  SELENOMETHIONINE                                   
HET    MSE  A  58       8                                                       
HET    MSE  A  98       8                                                       
HET    2ZC  A 180       9                                                       
HET    MSE  A 245       8                                                       
HET    MSE  B  98       8                                                       
HET    2ZC  B 180       7                                                       
HET    MSE  B 245       8                                                       
HET     CL  A 301       1                                                       
HET     CL  A 302       1                                                       
HET     CL  A 303       1                                                       
HET    GOL  B 301       6                                                       
HET     CL  B 302       1                                                       
HET    FMT  B 303       3                                                       
HET     CL  B 304       1                                                       
HET     CL  B 305       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     2ZC O-{[4-(2-AMINOETHYL)PHENYL]SULFONYL}-L-SERINE                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     FMT FORMIC ACID                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   1  2ZC    2(C11 H16 N2 O5 S)                                           
FORMUL   3   CL    6(CL 1-)                                                     
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   8  FMT    C H2 O2                                                      
FORMUL  11  HOH   *472(H2 O)                                                    
HELIX    1   1 PRO A   63  ALA A   66  5                                   4    
HELIX    2   2 GLY A  103  ASN A  107  5                                   5    
HELIX    3   3 SER A  111  ASP A  116  1                                   6    
HELIX    4   4 LYS A  117  ALA A  120  5                                   4    
HELIX    5   5 ASN A  121  ARG A  129  1                                   9    
HELIX    6   6 SER A  152  TYR A  167  1                                  16    
HELIX    7   7 2ZC A  180  LEU A  194  1                                  15    
HELIX    8   8 GLY A  209  GLY A  217  1                                   9    
HELIX    9   9 CYS A  218  VAL A  223  5                                   6    
HELIX   10  10 PRO A  238  CYS A  251  1                                  14    
HELIX   11  11 TRP A  271  SER A  276  1                                   6    
HELIX   12  12 ASP A  282  SER A  289  1                                   8    
HELIX   13  13 PRO B   63  ALA B   66  5                                   4    
HELIX   14  14 GLY B  103  ASN B  107  5                                   5    
HELIX   15  15 SER B  111  ASP B  116  1                                   6    
HELIX   16  16 LYS B  117  ALA B  120  5                                   4    
HELIX   17  17 ASN B  121  ARG B  129  1                                   9    
HELIX   18  18 SER B  152  TYR B  167  1                                  16    
HELIX   19  19 2ZC B  180  LEU B  194  1                                  15    
HELIX   20  20 GLY B  209  GLY B  217  1                                   9    
HELIX   21  21 CYS B  218  VAL B  223  5                                   6    
HELIX   22  22 PRO B  238  CYS B  251  1                                  14    
HELIX   23  23 TRP B  271  SER B  276  1                                   6    
HELIX   24  24 ASP B  282  SER B  289  1                                   8    
SHEET    1   A 8 LEU A  68  ARG A  71  0                                        
SHEET    2   A 8 PHE A  82  TYR A  85 -1  O  GLU A  84   N  SER A  69           
SHEET    3   A 8 VAL A 139  PRO A 143 -1  O  VAL A 140   N  TYR A  85           
SHEET    4   A 8 ALA A  95  TRP A 101  1  N  MSE A  98   O  VAL A 139           
SHEET    5   A 8 VAL A 169  LEU A 179  1  O  TYR A 175   N  LEU A  97           
SHEET    6   A 8 ALA A 201  ILE A 205  1  O  ILE A 205   N  GLY A 178           
SHEET    7   A 8 ILE A 225  GLY A 230  1  O  TRP A 226   N  ALA A 202           
SHEET    8   A 8 GLN A 258  TYR A 263  1  O  GLN A 259   N  GLY A 227           
SHEET    1   B 8 LEU B  68  ARG B  71  0                                        
SHEET    2   B 8 PHE B  82  TYR B  85 -1  O  GLU B  84   N  SER B  69           
SHEET    3   B 8 VAL B 139  PRO B 143 -1  O  VAL B 140   N  TYR B  85           
SHEET    4   B 8 ALA B  95  TRP B 101  1  N  MSE B  98   O  VAL B 139           
SHEET    5   B 8 VAL B 169  LEU B 179  1  O  TYR B 175   N  LEU B  97           
SHEET    6   B 8 ALA B 201  ILE B 205  1  O  ILE B 205   N  GLY B 178           
SHEET    7   B 8 ILE B 225  GLY B 230  1  O  TRP B 226   N  ALA B 202           
SHEET    8   B 8 GLN B 258  TYR B 263  1  O  THR B 261   N  GLY B 227           
SSBOND   1 CYS A  150    CYS A  181                          1555   1555  2.06  
SSBOND   2 CYS A  218    CYS A  251                          1555   1555  2.04  
SSBOND   3 CYS B  150    CYS B  181                          1555   1555  2.07  
SSBOND   4 CYS B  218    CYS B  251                          1555   1555  2.05  
LINK         C   ALA A  57                 N   MSE A  58     1555   1555  1.33  
LINK         C   MSE A  58                 N   VAL A  59     1555   1555  1.33  
LINK         C   LEU A  97                 N   MSE A  98     1555   1555  1.33  
LINK         C   MSE A  98                 N   VAL A  99     1555   1555  1.33  
LINK         C   PRO A 244                 N   MSE A 245     1555   1555  1.33  
LINK         C   MSE A 245                 N   ASN A 246     1555   1555  1.34  
LINK         C   LEU B  97                 N   MSE B  98     1555   1555  1.34  
LINK         C   MSE B  98                 N   VAL B  99     1555   1555  1.33  
LINK         C   PRO B 244                 N   MSE B 245     1555   1555  1.34  
LINK         C   MSE B 245                 N   ASN B 246     1555   1555  1.34  
LINK         C   LEU A 179                 N   2ZC A 180     1555   1555  1.33  
LINK         C   2ZC A 180                 N   CYS A 181     1555   1555  1.33  
LINK         C   LEU B 179                 N   2ZC B 180     1555   1555  1.32  
LINK         C   2ZC B 180                 N   CYS B 181     1555   1555  1.32  
CISPEP   1 GLN A  253    PRO A  254          0        -0.52                     
CISPEP   2 GLN B  253    PRO B  254          0         3.26                     
SITE     1 AC1  6 ARG A 273  ALA A 279  HOH A 425  ARG B 273                    
SITE     2 AC1  6 ALA B 279  HOH B 433                                          
SITE     1 AC2  2 ARG A 125  ARG A 129                                          
SITE     1 AC3  1 GLY A 148                                                     
SITE     1 AC4  4 ARG A  62  GLY B 148  HOH B 592  HOH B 607                    
SITE     1 AC5  1 ARG B 129                                                     
SITE     1 AC6  2 ARG B 210  ALA B 237                                          
SITE     1 AC7  1 ALA B 153                                                     
SITE     1 AC8  1 ARG B 273                                                     
CRYST1   77.935  146.084   68.720  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012831  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006845  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014552        0.00000                         
TER    1863      ARG A 292                                                      
TER    3719      ARG B 292                                                      
MASTER      626    0   15   24   16    0    9    6 4071    2   87   44          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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